The Ebola virus can cause hemorrhagic fever that is usually fatal. According to the Center for Disease Control and Prevention, outbreaks have caused more than 1,000 deaths, mostly in Central Africa, since it was first recognized in 1976. Approved treatments for these infections are currently lacking. The Ebola VP35 protein is multifunctional, acting as a component of the viral RNA polymerase complex, a viral assembly factor, and an inhibitor of host interferon (IFN) production. Mutation of select basic residues within the C-terminal half of VP35 abrogates its dsRNA-binding activity, impairs VP35-mediated IFN antagonism, and attenuates EBOV growth in vitro and in vivo. Because VP35 contributes to viral escape from host innate immunity and is required for EBOV virulence, understanding the structural basis for VP35 dsRNA binding, which correlates with suppression of IFN activity, is of high importance.
A team led by Gaya Amarasinghe, an assistant professor in biochemistry, biophysics and molecular biology, has recently solved the structure from a key part of the Ebola protein known as VP35. This protien interferes with the natural resistance of host cells against viral infections. when viruses infect cells, the host immune system can fight to eventually clear the virus. But with Ebola infections, the ability of the host to mount a defense against the invading virus is lost
I think this if not controlled will be like deadly epidemic AIDS (and even worst than this...), because of the fact that the VP35 protein interferes with the host's innate immune pathways that form the first line of defense against pathogens. With the advent of technologies like combination of X-ray crystallography and nucleic magnetic resonance spectroscopy the team has achieved the structure by using non-infectious protein samples. Hope this template (known structure) will help the drug discoverers to identify and design drugs that potentially bind with VP35 and their by substantiate anti-viral drug discovery. Congrats to Gaya Amarashinghe and his team. More ....
A team led by Gaya Amarasinghe, an assistant professor in biochemistry, biophysics and molecular biology, has recently solved the structure from a key part of the Ebola protein known as VP35. This protien interferes with the natural resistance of host cells against viral infections. when viruses infect cells, the host immune system can fight to eventually clear the virus. But with Ebola infections, the ability of the host to mount a defense against the invading virus is lost
I think this if not controlled will be like deadly epidemic AIDS (and even worst than this...), because of the fact that the VP35 protein interferes with the host's innate immune pathways that form the first line of defense against pathogens. With the advent of technologies like combination of X-ray crystallography and nucleic magnetic resonance spectroscopy the team has achieved the structure by using non-infectious protein samples. Hope this template (known structure) will help the drug discoverers to identify and design drugs that potentially bind with VP35 and their by substantiate anti-viral drug discovery. Congrats to Gaya Amarashinghe and his team. More ....
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